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Literature summary for 3.4.21.62 extracted from

  • Gololobov,M.Y.; Morozova, I.P.; Vojushina, T.L.; Timokhina, E.A.; Stepanov, V.M.
    Subtilisin from Bacillus subtilis strain 72. The influence of substrate structure, temperature and pH on catalytic properties (1992), Biochim. Biophys. Acta, 1118, 267-276.
    View publication on PubMed
Search for more literature for 3.4.21.62

General Stability

General Stability Organism
Substrate binding stabilizes the enzyme Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information the temperature dependence of the kinetics and thermodynamic parameters suggest that the enzyme exists in two, i.e. cold and hot forms, at 22°C the cold form turns into the hot one possibly owing to a conformational change Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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-
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Bacillus subtilis 72
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information influence of substrate structure of N-protected peptide nitroanilides of the types: benzyloxycarbonyl-A2-A1 4-nitroanilide, benzyloxycarbonyl-A3-A2-A1 4-nitroanilide, benzyloxycarbonyl-A4-A3-A2-A1 4-nitroanilide, subsite S1 is of broad selectivity: preference for hydrophobic amino acid residues (i.e. leucine and phenylalanine) the beta-branched and the basic amino acid residues cannot interact with the S1 subsite and the hydrolysis of the corresponding peptides occurs exclusively at the A2-A1 bond. If S1/A1 interactions are weak (Ala, norvaline, norleucine) the amino acid residue A1 can interact with subsites S1 and S1' resulting in the hydrolysis of two bonds (A1 4-nitroanilide and A2-A1). The subsite S2 reveals a preference for small amino acid residues Bacillus subtilis ?
-
 ?
additional information influence of substrate structure of N-protected peptide nitroanilides of the types: benzyloxycarbonyl-A2-A1 4-nitroanilide, benzyloxycarbonyl-A3-A2-A1 4-nitroanilide, benzyloxycarbonyl-A4-A3-A2-A1 4-nitroanilide, subsite S1 is of broad selectivity: preference for hydrophobic amino acid residues (i.e. leucine and phenylalanine) the beta-branched and the basic amino acid residues cannot interact with the S1 subsite and the hydrolysis of the corresponding peptides occurs exclusively at the A2-A1 bond. If S1/A1 interactions are weak (Ala, norvaline, norleucine) the amino acid residue A1 can interact with subsites S1 and S1' resulting in the hydrolysis of two bonds (A1 4-nitroanilide and A2-A1). The subsite S2 reveals a preference for small amino acid residues Bacillus subtilis 72 ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 stable below Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Bacillus subtilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5 9 stable Bacillus subtilis